Date published: 2025-9-20

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JAML Inhibitors

Chemical inhibitors of JAML can exert their effects through interference with various cellular signaling pathways that are crucial for the protein's function in cell adhesion and migration. LY294002 and Wortmannin are both inhibitors of PI3K, a kinase that is vital for a multitude of cellular functions including the regulation of cell adhesion. By inhibiting PI3K, these chemicals can disrupt the downstream signaling necessary for the proper functioning of JAML within the cellular adhesion complexes. Similarly, PP2, as a Src family kinase inhibitor, can reduce the tyrosine phosphorylation of proteins involved in cell adhesion, potentially compromising the adhesive and signaling functions where JAML is active. The inhibition of p38 MAPK by SB203580 could decrease the cell's response to inflammatory stimuli and stress, which might be necessary for the regulation of cell adhesion and migration involving JAML.

Furthermore, PD98059 and U0126 target the MEK/ERK pathway, a critical route for transmitting signals that regulate cell proliferation, differentiation, and adhesion – processes where JAML is implicated. By blocking this pathway, these inhibitors can reduce the cellular activities that depend on JAML's function. SP600125, a JNK inhibitor, can impair inflammatory signaling pathways and cell migration mechanisms, potentially affecting JAML's role in these processes. Xestospongin C disrupts calcium signaling by inhibiting the IP3 receptor, leading to reduced Ca2+ release; since calcium signaling is integral to cell adhesion and motility, this can indirectly inhibit JAML's function. ML7 and Y-27632 target myosin light chain kinase and ROCK, respectively, which are both central to cytoskeletal dynamics and cell shape changes, processes in which JAML activity is essential. Without the proper regulation of the cytoskeleton, JAML's role in cell adhesion could be impaired. Moreover, Gö6976 acts as a protein kinase C inhibitor, potentially affecting cell junction formation, an area where JAML has been shown to be active. Lastly, BAPTA, by chelating calcium, can disrupt intracellular calcium signaling pathways, which are vital for cell adhesion and migration, thereby influencing JAML's functional involvement in these processes.

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